Lysine deacetylases (KDACs) catalyze the hydrolysis of ε-N-acetyl lysine residues in proteins to generate an unmodified lysine residue and acetate. KDACs play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Perturbations in this process have been linked to diseases, including cancer and inflammation. While thousands of acetylated proteins have been identified, little information is known concerning the specificity profiles of KDACs and the role of several conserved active site residues in determining that specificity. In this study, selected residues were mutated in different deacetylates with the goal of expressing and purifying the resulting proteins to evaluate the effect of the mutations on the enzyme’s activity, which was measured using a panel of model peptide substrates. The results provide insight into the selectivity and mechanism of KDACs.

Probing the substrate specificity of lysine deacetylases using mutagenesis

249th National Meeting (2015)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.